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Specific Binding of...
Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species
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- Tiiman, Ann (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Luo, Jinghui (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,University of Oxford, UK
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- Wallin, Cecilia (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Olsson, Lisa (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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Lindgren, Joel (author)
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- Jarvet, Jϋri (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,The National Institute of Chemical Physics and Biophysics, Estonia
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Roos, Per (author)
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- Sholts, Sabrina B. (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,National Museum of Natural History, USA
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Rahimipour, Shai (author)
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Abrahams, Jan Pieter (author)
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- Eriksson Karlström, Amelie (author)
- KTH,Proteinteknologi
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- Gräslund, Astrid (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Wärmländer, Sebastian K. T. S. (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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(creator_code:org_t)
- IOS Press, 2016
- 2016
- English.
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In: Journal of Alzheimer's Disease. - : IOS Press. - 1387-2877 .- 1875-8908. ; 54:3, s. 971-982
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https://urn.kb.se/re...
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https://doi.org/10.3...
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Abstract
Subject headings
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- Aggregation of the amyloid-beta (A beta) peptide into insoluble plaques is a major factor in Alzheimer's disease (AD) pathology. Another major factor in AD is arguably metal ions, as metal dyshomeostasis is observed in AD patients, metal ions modulate A beta aggregation, and AD plaques contain numerous metals including redox-active Cu and Fe ions. In vivo, A beta is found in various cellular locations including membranes. So far, Cu(II)/A beta interactions and ROS generation have not been investigated in a membrane environment. Here, we study Cu(II) and Zn(II) interactions with A beta bound to SDS micelles or to engineered aggregation-inhibiting molecules (the cyclic peptide CP-2 and the Z(A beta 3)(12-58) Y18L Affibody molecule). In all studied systems the A beta N-terminal segment was found to be unbound, unstructured, and free to bind metal ions. In SDS micelles, A beta was found to bind Cu(II) and Zn(II) with the same ligands and the same K-D as in aqueous solution. ROS was generated in all Cu(II)/A beta complexes. These results indicate that binding of A beta to membranes, drugs, and other entities that do not interact with the A beta N-terminal part, appears not to compromise the N-terminal segment's ability to bind metal ions, nor impede the capacity of N-terminally bound Cu(II) to generate ROS.
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Neurologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Neurology (hsv//eng)
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Keyword
- Alzheimer's disease
- copper-binding protein
- hydrogen peroxide
- membrane chemistry
- neurodegeneration
- protein aggregation
- Biophysics
- biofysik
Publication and Content Type
- ref (subject category)
- art (subject category)
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To the university's database
- By the author/editor
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Tiiman, Ann
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Luo, Jinghui
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Wallin, Cecilia
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Olsson, Lisa
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Lindgren, Joel
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Jarvet, Jϋri
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show more...
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Roos, Per
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Sholts, Sabrina ...
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Rahimipour, Shai
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Abrahams, Jan Pi ...
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Eriksson Karlstr ...
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Gräslund, Astrid
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Wärmländer, Seba ...
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- About the subject
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Chemical Science ...
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Clinical Medicin ...
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and Neurology
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
- Articles in the publication
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Journal of Alzhe ...
- By the university
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Stockholm University
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Royal Institute of Technology
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Karolinska Institutet